PRTN3 cleaves CAMP(31-170) to generate CAMP(134-170)

Stable Identifier
Reaction [omitted]
Homo sapiens
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Cathelicidin (CAMP, LL-37 and hCAP), is a major protein in specific granules of neutrophils (Sorensen O et al. 1997). CAMP is also present in subpopulations of lymphocytes and monocytes, squamous epithelial cells and keratinocytes (Agerberth B et al. 2000; Frohm M et al. 1997; Frohm Nilsson M et al. 1999). CAMP is synthesized as preproprotein (Zanetti M et al. 1995). After removal of the signal peptide, CAMP(31-170) is stored in granules as an inactive proform (Sorensen OE et al. 2001). CAMP (31-170) was shown to be processed extracellularly to the active antimicrobial peptide LL-37 (CAMP(134-170)) by proteinase 3 (PRTN3) (Sorensen OE et al. 2001).

Literature References
PubMed ID Title Journal Year
11389039 Human cathelicidin, hCAP-18, is processed to the antimicrobial peptide LL-37 by extracellular cleavage with proteinase 3

Johnsen, AH, Sørensen, OE, Borregaard, N, Follin, P, Tjabringa, GS, Hiemstra, PS, Calafat, J

Blood 2001
Catalyst Activity

serine-type endopeptidase activity of PRTN3 [extracellular region]

Orthologous Events
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